Sterol Methyltransferase: Functional Analysis of Highly Conserved Residues by Site-Directed Mutagenesis

Sterol methyltransferase (SMT), the enzyme from Saccharomyces cerevisiae that catalyzes the conversion of sterol acceptor in the presence of AdoMet to C-24 methylated sterol and AdoHcy, was analyzed for amino acid residues that contribute to C-methylation activity. Site-directed mutagenesis of nine...

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Veröffentlicht in:	Biochemistry (Easton) 2004-01, Vol.43 (2), p.569-576
Hauptverfasser:	Nes, W. David, Jayasimha, Pruthvi, Zhou, Wenxu, Kanagasabai, Ragu, Jin, Changxiao, Jaradat, Tahhan T, Shaw, Robert W, Bujnicki, Janusz M
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartic Acid - genetics Catalysis Circular Dichroism Conserved Sequence - genetics Glutamic Acid - genetics Methyltransferases - chemistry Methyltransferases - genetics Models, Chemical Models, Molecular Mutagenesis, Site-Directed Recombinant Proteins - chemistry Recombinant Proteins - genetics Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Sequence Homology, Amino Acid Substrate Specificity
Online-Zugang:	Volltext
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